ArticleActa crystallographica. Section F, Structural biology communications2017
Crystal structure of type II NADH:quinone oxidoreductase from Caldalkalibacillus thermarum with an improved resolution of 2.15 Å.
Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Inhibitors of Type II NADH Dehydrogenase Enzyme: A Review.Current protein & peptide science · 2025Review
- The respiratory chain ofFrontiers in microbiology · 2024Article
- Structure of mycobacterial CIIIeLife · 2021Article
- Article
- Structure of the NDH-2 - HQNO inhibited complex provides molecular insight into quinone-binding site inhibitors.Biochimica et biophysica acta. Bioenergetics · 2018Article
- Ubiquinone binding site of yeast NADH dehydrogenase revealed by structures binding novel competitive- and mixed-type inhibitors.Scientific reports · 2018Article
- Breakthroughs in the development of antibiotics, antifungals and antiparasitics targeting the pathogens' respiratory chain.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
7 authors.
Funding
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Abstract
Type II NADH:quinone oxidoreductase (NDH-2) is a respiratory enzyme found in the electron-transport chain of many species, with the exception of mammals. It is a 40-70 kDa single-subunit monotopic membrane protein that catalyses the oxidation of NADH and the reduction of quinone molecules via the cofactor FAD. NDH-2 is a promising new target for drug development given its essential role in many bacterial species and intracellular parasites. Only two bacterial NDH-2 structures have been reported and these structures are at moderate resolution (2.3-2.5 Å). In this communication, a new crystallization platform is reported that produced high-quality NDH-2 crystals that diffracted to high resolution (2.15 Å). The high-resolution NDH-2 structure was used for in silico quinone substrate-docking studies to investigate the binding poses of menadione and ubiquinone molecules. These studies revealed that a very limited number of molecular interactions occur at the quinone-binding site of NDH-2. Given that the conformation of the active site is well defined, this high-resolution structure is potentially suitable for in silico inhibitor-compound screening and ligand-docking applications.
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